Abstract
The x-ray diffraction study of the C-terminally unprotected tripeptide benzyloxy-carbonyl-L-alanyl-alpha-aminoisobutyl-alpha- aminoisobutylic acid (Z-L-Ala-Aib-Aib-OH) has shown that the molecule adopts a consecutive type III beta-turn, which characterizes a right-handed 3(10) helix. A very weak 4----1 intramolecular hydrogen bond with the long N...O distance of 3.32 A, and a unique "oxy analogue" of the 4----1 hydrogen bond wih the O...O distance of 2.77 A, were observed. The stability of the observed conformation with the asymmetric Aib residues was theoretically evaluated by a conformation-energy calculation. The stereochemical characteristics of Aib and Ala residues were made clear by a comparison of the conformations of the short peptides containing both Aib and Ala residues.
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